Glycerol kinase (P0A6F3)

Identification
Name:Glycerol kinase
Synonyms:
  • ATP:glycerol 3-phosphotransferase
  • Glycerokinase
  • GK
Gene Name:glpK
Enzyme Class:
Biological Properties
General Function:Involved in phosphotransferase activity, alcohol group as acceptor
Specific Function:Key enzyme in the regulation of glycerol uptake and metabolism
Cellular Location:Not Available
SMPDB Pathways:
  • glycerol metabolism PW000914
  • glycerol metabolism II PW000915
  • glycerol metabolism III (sn-glycero-3-phosphoethanolamine) PW000916
  • glycerol metabolism IV (glycerophosphoglycerol) PW000917
  • glycerol metabolism V (glycerophosphoserine) PW000918
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Glycerol ↔ 1.0ADP + 1.0Glycerol 3-phosphate + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Glycerol ↔ 1.0ADP + 1.0Glycerol 3-phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb
1.0Glycerol + 1.0Adenosine triphosphate → 1.0Hydrogen ion + 1.0Adenosine diphosphate + 1.0Glycerol 3-phosphate + 1.0ADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Glycerol ↔ 1.0ADP + 1.0Glycerol 3-phosphate + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Glycerol → 1.0ADP + 1.0Glycerol 3-phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00131GlycerolMetaboCard
ECMDB00126Glycerol 3-phosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
GO Classification:
Function
catalytic activity
glycerol kinase activity
kinase activity
phosphotransferase activity, alcohol group as acceptor
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
alcohol metabolic process
alditol metabolic process
carbohydrate metabolic process
glycerol metabolic process
glycerol-3-phosphate metabolic process
metabolic process
polyol metabolic process
primary metabolic process
small molecule metabolic process
Gene Properties
Blattner:b3926
Gene OrientationCounterclockwise
Centisome Percentage:88.66
Left Sequence End4113737
Right Sequence End4115245
Gene Sequence:
>1509 bp
ATGGCTATTAGCACACCGATGTTGGTGACATTTTGTGTCTATATCTTTGGCATGATATTG
ATTGGGTTTATCGCCTGGCGATCAACGAAAAACTTTGACGACTATATTCTGGGCGGTCGT
AGTCTTGGGCCATTCGTGACGGCATTATCGGCGGGTGCGTCGGATATGAGCGGCTGGCTG
TTAATGGGGTTGCCGGGCGCTGTTTTTCTTTCCGGGATTTCCGAAAGCTGGATCGCCATT
GGCCTGACATTAGGCGCGTGGATTAACTGGAAGCTGGTGGCCGGGCGGTTGCGTGTGCAT
ACCGAATACAACAATAACGCCTTAACACTGCCGGATTATTTCACCGGGCGCTTTGAAGAT
AAAAGCCGCATTTTGCGCATTATCTCTGCGCTGGTTATTTTGCTGTTCTTCACCATTTAT
TGCGCTTCGGGCATTGTGGCAGGCGCGCGTCTGTTTGAAAGTACCTTTGGCATGAGCTAC
GAAACGGCTCTGTGGGCGGGCGCTGCGGCGACGATCCTTTACACCTTTATTGGCGGTTTC
CTCGCGGTGAGCTGGACTGACACTGTACAGGCCAGCCTGATGATTTTTGCCCTGATCCTG
ACGCCGGTTATCGTCATTATCAGTGTCGGTGGCTTTGGTGACTCGCTGGAAGTGATCAAA
CAAAAGAGCATCGAAAACGTTGATATGCTCAAAGGTCTGAACTTTGTTGCCATTATCTCA
CTGATGGGTTGGGGGCTGGGTTACTTCGGGCAGCCGCACATTCTGGCGCGTTTTATGGCG
GCGGATTCTCACCACAGCATTGTCCATGCGCGTCGTATTAGTATGACCTGGATGATCCTC
TGCCTGGCAGGGGCGGTGGCTGTCGGCTTCTTTGGGATTGCTTACTTTAACGATCATCCG
GCGTTGGCTGGTGCGGTAAATCAGAACGCCGAGCGTGTGTTTATCGAACTGGCGCAAATT
CTGTTTAACCCGTGGATTGCCGGGATTCTGCTGTCGGCAATTCTGGCGGCGGTAATGTCA
ACCTTAAGTTGCCAGCTGCTGGTGTGCTCCAGTGCGATTACCGAAGATTTGTACAAAGCG
TTTCTGCGTAAACATGCCAGCCAGAAAGAGCTGGTGTGGGTAGGGCGTGTGATGGTGCTG
GTGGTGGCGCTGGTGGCGATTGCGCTGGCGGCAAACCCGGAAAACCGCGTGCTGGGCTTA
GTGAGCTACGCGTGGGCAGGCTTTGGCGCGGCGTTTGGTCCAGTGGTGCTGTTCTCGGTG
ATGTGGTCACGCATGACGCGTAACGGTGCGCTGGCGGGGATGATCATCGGTGCGCTGACG
GTTATCGTCTGGAAACAGTTCGGCTGGCTGGGACTGTACGAAATTATTCCGGGCTTTATC
TTCGGCAGTATTGGGATTGTAGTGTTTAGTTTGCTGGGTAAAGCGCCGTCAGCGGCGATG
CAAAAACGCTTTGCCGAGGCCGATGCGCACTATCATTCGGCTCCGCCGTCACGGTTGCAG
GAAAGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:502
Protein Molecular Weight:56230
Protein Theoretical pI:5
PDB File:1BOT
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glycerol kinase
MTEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSST
LVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDG
LEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVH
VTDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPI
SGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVN
YALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPY
ARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLM
QFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTER
NYRYAGWKKAVKRAMAWEEHDE
References
External Links:
ResourceLink
Uniprot ID:P0A6F3
Uniprot Name:GLPK_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651504
PDB ID:1BOT
Ecogene ID:EG10398
Ecocyc:EG10398
ColiBase:b3926
Kegg Gene:b3926
EchoBASE ID:EB0393
CCDB:GLPK_ECOLI
BacMap:16131764
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Bystrom, C. E., Pettigrew, D. W., Branchaud, B. P., O'Brien, P., Remington, S. J. (1999). "Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion." Biochemistry 38:3508-3518. Pubmed: 10090737
  • Feese, M. D., Faber, H. R., Bystrom, C. E., Pettigrew, D. W., Remington, S. J. (1998). "Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation." Structure 6:1407-1418. Pubmed: 9817843
  • Feese, M., Pettigrew, D. W., Meadow, N. D., Roseman, S., Remington, S. J. (1994). "Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation." Proc Natl Acad Sci U S A 91:3544-3548. Pubmed: 8170944
  • Gonzalez-Gil, G., Bringmann, P., Kahmann, R. (1996). "FIS is a regulator of metabolism in Escherichia coli." Mol Microbiol 22:21-29. Pubmed: 8899705
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Hurley, J. H., Faber, H. R., Worthylake, D., Meadow, N. D., Roseman, S., Pettigrew, D. W., Remington, S. J. (1993). "Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase." Science 259:673-677. Pubmed: 8430315
  • Muramatsu, S., Mizuno, T. (1989). "Nucleotide sequence of the region encompassing the glpKF operon and its upstream region containing a bent DNA sequence of Escherichia coli." Nucleic Acids Res 17:4378. Pubmed: 2544860
  • Ormo, M., Bystrom, C. E., Remington, S. J. (1998). "Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate." Biochemistry 37:16565-16572. Pubmed: 9843423
  • Pettigrew, D. W., Liu, W. Z., Holmes, C., Meadow, N. D., Roseman, S. (1996). "A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo." J Bacteriol 178:2846-2852. Pubmed: 8631672
  • Pettigrew, D. W., Ma, D. P., Conrad, C. A., Johnson, J. R. (1988). "Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme." J Biol Chem 263:135-139. Pubmed: 2826434
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018
  • Weissenborn, D. L., Wittekindt, N., Larson, T. J. (1992). "Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12." J Biol Chem 267:6122-6131. Pubmed: 1372899